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Database: UniProt
Entry: B4WRL4_SYNS7
LinkDB: B4WRL4_SYNS7
Original site: B4WRL4_SYNS7 
ID   B4WRL4_SYNS7            Unreviewed;      1177 AA.
AC   B4WRL4;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=Transcription-repair-coupling factor {ECO:0000256|HAMAP-Rule:MF_00969};
DE            Short=TRCF {ECO:0000256|HAMAP-Rule:MF_00969};
DE            EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_00969};
GN   Name=mfd {ECO:0000256|HAMAP-Rule:MF_00969};
GN   ORFNames=S7335_2553 {ECO:0000313|EMBL:EDX84855.1};
OS   Synechococcus sp. (strain ATCC 29403 / PCC 7335).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=91464 {ECO:0000313|EMBL:EDX84855.1, ECO:0000313|Proteomes:UP000005766};
RN   [1] {ECO:0000313|EMBL:EDX84855.1, ECO:0000313|Proteomes:UP000005766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29403 / PCC 7335 {ECO:0000313|Proteomes:UP000005766};
RA   Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA   Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Couples transcription and DNA repair by recognizing RNA
CC       polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent
CC       release of RNAP and its truncated transcript from the DNA, and
CC       recruitment of nucleotide excision repair machinery to the damaged
CC       site. {ECO:0000256|HAMAP-Rule:MF_00969}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the helicase family.
CC       RecG subfamily. {ECO:0000256|HAMAP-Rule:MF_00969}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the UvrB family.
CC       {ECO:0000256|HAMAP-Rule:MF_00969}.
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DR   EMBL; DS989904; EDX84855.1; -; Genomic_DNA.
DR   RefSeq; WP_006454601.1; NZ_DS989904.1.
DR   AlphaFoldDB; B4WRL4; -.
DR   STRING; 91464.S7335_2553; -.
DR   eggNOG; COG1197; Bacteria.
DR   HOGENOM; CLU_005122_1_3_3; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000005766; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IEA:UniProtKB-UniRule.
DR   CDD; cd17991; DEXHc_TRCF; 1.
DR   Gene3D; 2.40.10.170; -; 1.
DR   Gene3D; 3.40.50.11180; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 3.30.2060.10; Penicillin-binding protein 1b domain; 1.
DR   Gene3D; 3.90.1150.50; Transcription-repair-coupling factor, D7 domain; 1.
DR   HAMAP; MF_00969; TRCF; 1.
DR   InterPro; IPR003711; CarD-like/TRCF_RID.
DR   InterPro; IPR036101; CarD-like/TRCF_RID_sf.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR004576; Mfd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR047112; RecG/Mfd.
DR   InterPro; IPR037235; TRCF-like_C_D7.
DR   InterPro; IPR005118; TRCF_C.
DR   InterPro; IPR041471; UvrB_inter.
DR   NCBIfam; TIGR00580; mfd; 1.
DR   PANTHER; PTHR47964; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR47964:SF1; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR   Pfam; PF02559; CarD_TRCF_RID; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF03461; TRCF; 1.
DR   Pfam; PF17757; UvrB_inter; 1.
DR   SMART; SM01058; CarD_TRCF; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00982; TRCF; 1.
DR   SUPFAM; SSF141259; CarD-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR   SUPFAM; SSF143517; TRCF domain-like; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00969}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_00969};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_00969};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00969}; Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00969};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00969}; Reference proteome {ECO:0000313|Proteomes:UP000005766}.
FT   DOMAIN          643..804
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          829..981
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1177 AA;  132119 MW;  C2B67B63B468336E CRC64;
     MAFSSITRAI ARSPLAQELV AKLEKQQTLT ITGAPRLPKG LVSSALAQTQ NKPMLVVTAT
     LEEAGRWSAQ LEAMGWATVA FYPTSESSPY DVFDPESELI WGQLQVLSDL INGKANPENM
     PLGSKHLGTM AIVTTERALQ PHLPPVEAFR PYCLEITLGM ELNLKDLGLS LAKLGYEKVS
     SVEVEGQWSQ RGDIIDVFPV AAELPVRMEL FGDELERLRE FDPANQRSLD KIEALLLTTT
     DYGPLILSAL EEKELLEDLL TEESQETFAA TGKIEGARRF MGLAFESPAS ILDYLPDDTL
     VVIDEPAQCL AHAERWIETV EDRWQEALDA FEADVEIQLP SGGLPKVHRP FSQALEEIEL
     FQRIEISELA EEGVGLNLAS RPVPILPHQF GKLADILKEE RDRKFFPWLI SAQPSRSVAL
     LQEHDCPAQF IPNPKDFPAI DKLQNQRIPI AVKYSGLAEL EGFVLPTFRI VVVTDREFFG
     QHTLATPSYV RKRRRAASKQ VDPNKLRPKD YIVHRNHGIG QFLKLESLTV DKETREYLVI
     QYADGLLRVP VDQMGSLSRY RTSVEQRPQL NKMTGKAWEK TKGKARKAIK KVAVDLLKLY
     AQRSQMQGFT YPEDMPWQQE LEDSFPYNPT PDQLKATQDV KRDMESDRPM DRLVCGDVGF
     GKTEVALRAV FKAVTAGKQV ALLAPTTILT QQHYHTLKER FAPYPIQIGL LNRFRTAKER
     KDILLRLISG ELDVVVGTHQ LLGKTVKFKD LGLLVVDEEQ RFGVNQKEKI KAMKAQVDVL
     TLSATPIPRT LYMALSGVRE MSLITTPPPS RRPIKTHLSP YDPEKVRTAI RQELDRGGQI
     FYVVPRVEGI EEVAGRIREA VPGVRLAIAH GQMPEGELEA TMLTFSNGDA DLMVCTTIIE
     SGLDIPRVNT IIIEDSQKFG LSQLYQLRGR VGRSGIQAHA WLLFPKQNQL SDKARKRLRA
     IQEFTQLGSG YQLAMRDMEI RGIGNLLGAQ QSGQMEVIGF DLYMDMLEES IAEIRGQEIP
     QVDETQVDLK VTAFIPADYI PELDQKMSVY RSLVGASTRR ELIEIVADLN DHYGSLPSAV
     GQLVKVLELK QIAKPLGFSR IRTEDKQHVV LETPMEKPAW ALLHEKVPAH LRSRFVYAPG
     KVTVRGLGAV KPEKQIENLI EWLGHMQTAL PEPAFSR
//
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